Enzyme

Enzyme
Thomas Shafee · CC BY 4.0 · source
Name	Enzyme
Discovered	1833
Discoverer	Anselme Payen; Friedrich Wilhelm Kühne
Field	Biochemistry

Enzyme Enzymes are biological catalysts that accelerate chemical reactions in living systems, lowering activation energies to increase reaction rates. They are central to processes studied by Louis Pasteur's successors and researched in institutions like the Max Planck Society, Cold Spring Harbor Laboratory, and National Institutes of Health. Enzymology interfaces with techniques developed at Massachusetts Institute of Technology, University of Cambridge, and Stanford University and informs work by investigators such as J. B. S. Haldane, Emil Fischer, and Arthur Kornberg.

Introduction

Enzymes were first recognized in studies by Anselme Payen and characterized by Friedrich Wilhelm Kühne; later foundational contributions came from Emil Fischer's lock-and-key model and Daniel Koshland's induced-fit concept. Research programs at University of Oxford, Harvard University, California Institute of Technology, and Imperial College London expanded biochemical, structural, and genetic approaches. Methods including X-ray crystallography used at Royal Institution and cryo-electron microscopy advanced at Howard Hughes Medical Institute laboratories reveal active-site architecture central to catalysis.

Structure and Classification

Enzymes are typically proteins assembled from amino acids encoded by genes characterized in projects like the Human Genome Project and annotated in databases maintained by European Molecular Biology Laboratory and National Center for Biotechnology Information. Structural motifs discovered by groups at MRC Laboratory of Molecular Biology and Institut Pasteur include alpha helices and beta sheets; many enzymes require cofactors such as metal ions studied in work at Los Alamos National Laboratory and coenzymes like Nicotinamide adenine dinucleotide first described in research connected to Otto Warburg. Classification follows the Enzyme Commission system developed under the auspices of organizations like the International Union of Biochemistry and Molecular Biology: oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases. Structural families and folds have been cataloged in initiatives from European Bioinformatics Institute and research by Michael Levitt and David Baker.

Mechanism and Kinetics

Mechanistic studies draw on concepts introduced by Victor Henri, expanded by Brønsted and Arrhenius frameworks, and formalized in Michaelis–Menten kinetics based on work by Leonor Michaelis and Maud Menten. Kinetic parameters such as Km and Vmax are measured using assays developed in laboratories at Salk Institute and Wadsworth Center. Catalytic strategies include acid–base catalysis elucidated in investigations at University of Chicago, covalent catalysis characterized in studies by Christian Anfinsen's contemporaries, and transition-state stabilization probed by groups at University of California, San Francisco and Pierre-Gilles de Gennes-related physical chemistry groups. Single-molecule enzyme kinetics have been advanced through techniques from Bell Laboratories and imaging platforms at European Synchrotron Radiation Facility.

Regulation and Inhibition

Regulatory mechanisms include allosteric modulation first described in relation to hemoglobin by Monod, Wyman and Changeux and feedback inhibition exemplified in pathways elucidated by Edmund Beecher Wilson-era genetics and classical biochemical studies at Johns Hopkins University. Post-translational modifications such as phosphorylation were mapped in studies involving Edwin Krebs and Edmond Fischer and proteolytic activation pathways investigated by groups at Max Planck Institute for Biochemistry. Inhibitors range from reversible competitive molecules identified in pharmaceutical research at Pfizer and GlaxoSmithKline to irreversible mechanism-based inactivators developed with collaborations involving Eli Lilly and university spin-offs. Structural insights from X-ray and NMR studies at Brookhaven National Laboratory and Rutherford Appleton Laboratory guide rational inhibitor design.

Biological Roles and Applications

Enzymes catalyze central metabolic pathways mapped in research by laboratories at Weizmann Institute of Science and Rockefeller University, including glycolysis, the citric acid cycle, and oxidative phosphorylation studied in contexts of Otto Warburg and Hans Krebs. They perform DNA replication, repair, and transcription functions carried out by polymerases and nucleases investigated by researchers such as Kary Mullis and teams at EMBL-EBI. Enzymatic signaling roles involve kinases and phosphatases central to work at Memorial Sloan Kettering Cancer Center and Dana-Farber Cancer Institute. Applied biological uses include enzyme-linked assays pioneered in laboratories at Pasteur Institute and diagnostic platforms developed by companies like Roche and Abbott Laboratories.

Industrial and Medical Uses

Industrial biotechnology employs enzymes in processes commercialized by firms such as Novozymes and DuPont for detergents, biofuel production, and food processing; biocatalysis innovations stem from partnerships with BASF and academic groups at ETH Zurich. Medical applications include enzyme replacement therapies produced by biotechnology firms and clinical programs at Mayo Clinic and Cleveland Clinic for lysosomal storage disorders; antibiotics and antiviral drug design target enzyme active sites in development pipelines at Merck and Gilead Sciences. Enzymes underpin molecular diagnostics, including PCR-based tests commercialized following work at Cetus Corporation and clinical laboratories at Centers for Disease Control and Prevention.

Category:Biochemistry